Purification of transketolase from baker's yeast by an immunoadsorbent.
Baker's yeast transketolase has been purified by immunoaffinity chromatography on specific TK antibodies covalently linked to CNBr-agarose. Affinity chromatography allows a 480-fold purification of TK from yeast extracts and about 80% recovery of the original activity. The isolated enzyme has a specific activity of 12-60 U/mg and during polyacrylamide gel electrophoresis performed at pH 8.9 migrates as two protein bands possessing a transketolase activity which corresponds to two isoforms of the enzyme.
Tikhomirova
N K
NK
A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Kochetov
G A
GA
D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007163:Immunosorbent Techniques; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D014174:Transketolase / Q000302:isolation & purification* / Q000378:metabolism
D014174:Transketolase